Ohm intelligent car battery refuses to die

 

The Ohm is designed as a smarter form of car battery It's a terrible feeling. You're already late for wherever you're going, so you rush into the car and slam the door shut. You put the key in, give it the usual twist and ... nothing, not a peep. Dead battery. Many a driver has experienced this issue at one point or another, and most would prefer not to repeat it. The Ohm smart battery was designed to help make sure you never do. The car battery is one of those items that most people really don't want to think too much about. They want to replace it as infrequently as possible and then have it just work, every time, without fuss. It's no surprise, therefore, that the car battery is largely the big, heavy, electrochemical block that it was generations ago. It does its job pretty well, and you don't really have to think about it much. Silicon Valley startup Ohm Laboratories believes there's some room for improvement and new thinking, though. More than just a battery, its Ohm battery is an energy storage and management system in a battery-sized case. Its integrated processor monitors power level and automatically cuts power when the battery drops to a critical level. So if you accidentally leave your lights on, Ohm will shut itself down before going dead and then turn itself back on within about 30 seconds when you start up the car. The self shut-off system is a handy feature to have during the battery's effective life, but there's one dead battery issue it can't help with: end of life. That's why the battery also has a replacement warning system. The system beeps to let you know it's time for replacement, and Ohm says it works more quickly and accurately than the battery warning light on the dashboard. Unlike the lead acid construction of typical car batteries, Ohm uses a combination of lithium iron phosphate batteries and supercapacitors. It's the supercapacitors that deliver the quick burst of electricity for starting. The LiFePO4 batteries, in turn, keep the supercapacitors charged when the engine is off, so they're ready to go when you twist the key or punch the ignition button. Ohm says that the LiFePO4/supercapacitor configuration gives the battery a seven-year lifespan, which is around double that of the average lead acid battery. It also makes claims of better performance in cold weather. Assuming it doesn't gain any bulk before production, the Ohm is also a lot lighter than a lead acid battery. The estimated 6-lb (2.7-kg) weight looks light right off the bat, but when you compare it to the ~35 pounds (15.9 kg) a group size 35 lead acid battery weighs, it's downright feathery. That loss not only cuts down your vehicle's weight, it makes the Ohm easier to handle during replacement. While lighter internally, the Ohm's body is sized to slide into existing cars' battery wells and connect just like a lead acid car battery. The unit comes in two sizes – one designed to fit neatly in cars that accept group size 35 batteries and one designed for smaller battery wells. You can use the reference tool on Ohm's Indiegogo page to find out if the battery is a match for your car. Ohm designers admit one downside to their design: a small 10 Ah reserve capacity. This could be a problem if you rely on the battery to run electrical equipment and accessories with the engine off, and Ohm suggests sticking with a standard lead acid battery if that's the case. Thanks to the Ohm's self shut-off, at least you won't risk running the battery dead. The Ohm team says that it has tested its battery over thousands of miles but still has a lot of testing left to do on aspects like life cycle, temperature rating and battery management circuitry. Its numbers are not finalized, so the aforementioned seven-year lifespan, 10 Ah reserve capacity and 6-lb weight are still subject to change, as are the 500 peak cold cranking amps and -22 to 122° F (-30 to 50° C) operating range. Ohm has worked with the seed funders at Y Combinator and has turned toIndiegogo to raise the additional funding it needs to complete testing, finalize the design, purchase tooling and get production started. It is closing in on its US$50,000 goal with 23 days left to go and the lowest early bird pledge levels have sold out, but the Ohm battery is still available at $199, a $20 discount off the estimated retail price. That price is probably a lot higher than you'd spend on a lead acid battery at the local auto parts store, but if the Ohm performs as promised, it may be worth it. Source: Ohm

High iron intake may increase appetite, disease risk

 

Here's one more reason to cut down on the amount of red meat you eat. Using an animal model, researchers at Wake Forest Baptist Medical Center have found that dietary iron intake, equivalent to heavy red meat consumption, suppresses leptin, a hormone that regulates appetite. Iron is the one mineral that humans can't excrete, so the more iron that is consumed the greater the likelihood that leptin levels will drop, resulting in increased appetite and the potential to overeat. The study was recently published in the Journal of Clinical Investigation. "We showed that the amount of food intake increased in animals that had high levels of dietary iron," said Don McClain, M.D., Ph.D., director of the Center on Diabetes, Obesity and Metabolism at Wake Forest Baptist and senior author of the study. "In people, high iron, even in the high-normal range, has been implicated as a contributing factor to many diseases, including diabetes, fatty liver disease and Alzheimer's, so this is yet another reason not to eat so much red meat because the iron in red meat is more readily absorbed than iron from plants." In this study, male mice were fed high (2000 mg/kg) and low-normal (35 mg/kg) iron diets for two months, followed by measuring the levels of iron in fat tissue. The researchers observed a 215 percent increase of iron in the mice fed a high iron diet as compared to the mice fed the low normal diet. In addition, leptin levels in blood were 42 percent lower in mice on the high iron diet compared to those on the low normal diet. Results from the animal model were verified through ferritin blood tests from a large number of human participants in a previous clinical study. Ferritin blood tests measure the amount of iron stored in the body. The researchers showed that fat tissue responds to iron availability to adjust the expression of leptin, a major regulator of appetite, energy expenditure and metabolism. "We don't know yet what optimal iron tissue level is, but we are hoping to do a large clinical trial to determine if decreasing iron levels has any effect on weight and diabetes risk," McClain said. "The better we understand how iron works in the body, the better chance we have of finding new pathways that may be targets for the prevention and treatment of diabetes and other diseases." Funding for the study was provided by the Research Service of the Department of Veterans Affairs and the national Institutes of Health. This study was conducted at the University of Utah before McClain joined Wake Forest Baptist. Co-authors are Yan Gao, Ph.D., Zhonggang Li, M.S., Scott Gabrielsen, M.D., Ph.D., Judith A. Simcox, Ph.D., Soh-hyun Lee, Ph.D., Deborah Jones, B.S., Bob Cooksey, M.S., and Gregory Stoddard, Ph.D., of the University of Utah; William T. Cefalu, M.D., of Louisiana State University System. Story Source: The above post is reprinted from materials provided by Wake Forest Baptist Medical Center. Note: Materials may be edited for content and length. Journal Reference: Yan Gao, Zhonggang Li, J. Scott Gabrielsen, Judith A. Simcox, Soh-hyun Lee, Deborah Jones, Bob Cooksey, Gregory Stoddard, William T. Cefalu, Donald A. McClain. Adipocyte iron regulates leptin and food intake. Journal of Clinical Investigation, 2015; 10.1172/JCI81860 DOI: 10.1172/JCI81860

Structural Discoveries Could Aid in Better Drug Design

 

Scientists from The Scripps Research Institute Florida campus have uncovered the structural details of how some proteins interact to turn two different signals into a single integrated output. These new findings could aid future drug design by giving scientists an edge in fine tuning the signal between these partnered proteins -- and the drug's course of action. F. Scott Fitzgerald once said that the test of a first-rate intelligence is the ability to hold two opposed ideas in mind at the same time and still retain the ability to function. Now, scientists from the Florida campus of The Scripps Research Institute (TSRI) have found the biological equivalent of that idea or something very close. For the first time, they have uncovered the structural details of how some proteins interact to turn two different signals into a single integrated output. These new findings could aid future drug design by giving scientists an edge in fine tuning the signal between these partnered proteins -- and the drug's course of action. "Thyroid, vitamin D and retinoid receptors all rely on integrated signals -- their own signal plus a partner receptor," said TSRI Associate Professor Kendall Nettles, who led the study with TSRI colleague Associate Professor Douglas Kojetin. "These new findings will have important implications for drug design by clearly defining exactly how these signals become integrated, so we will be able to predict how changes in a drug's design could affect signaling." The study was published recently in the journal Nature Communications. Using a number of complementary technologies, including nuclear magnetic resonance (NMR), X-ray crystallography and hydrogen/deuterium exchange (HDX) mass spectrometry from the laboratory of Scripps Florida colleague Chair of the Department of Molecular Therapeutics Patrick R. Griffin, the scientists were able to determine the mechanism through which two signaling pathways become integrated. The study focused on a small subset of nuclear receptors, a large family of proteins that regulate gene expression in response to signals from various binding partners, including steroids and fats. Once receptors sense the presence of these binding partners, they send out new signals that initiate other cellular processes.   "Nuclear receptors bind different types of molecules, and some of these receptors physically interact with each other to integrate different signals," Kojetin said. "Earlier studies basically accepted this without any structural evidence for communication between receptors. This is the first time that anyone has looked at what's actually going on at the atomic level." The work was supported by the National Institutes of Health (grants DK101871, GM114420, GM063855, RR019077, RR027755, MH084512, GM084041, RR027270 and CA132022), the Frenchman's Creek Women for Cancer Research, the James and Esther King Biomedical Research Program, the Florida Department of Health and the State of Florida. Story Source: The above post is reprinted from materials provided by The Scripps Research Institute. Note: Materials may be edited for content and length. Journal Reference: Douglas J. Kojetin, Edna Matta-Camacho, Travis S. Hughes, Sathish Srinivasan, Jerome C. Nwachukwu, Valerie Cavett, Jason Nowak, Michael J. Chalmers, David P. Marciano, Theodore M. Kamenecka, Andrew I. Shulman, Mark Rance, Patrick R. Griffin, John B. Bruning, Kendall W. Nettles.Structural mechanism for signal transduction in RXR nuclear receptor heterodimers. Nature Communications, 2015; 6: 8013 DOI:10.1038/ncomms9013

Gut feeling restored by growth outside the body

 

University of Manchester scientists have bridged a gap between two separate pieces of small intestine kept alive outside the body, in an advance which could have implications for surgery in human adults and babies. It is not currently possible to study the intestine in embryos when inside the body, which holds back advances in treatment for conditions causing damage in infants. However, new techniques used by the researchers in this study have allowed organs to be kept alive and grown on supports which allow the absorption of nutrients. In the new research, two pieces of embryonic mouse intestine were placed on the supports with a small gap between them. A thread was inserted to link the two and the researchers observed the two pieces grow together to such an extent that in three quarters of the 36 tests, nerve signals were passed between them causing the now joined piece to operate as a single section of gut. Professor Adrian Woolf, from the University's Institute of Human Development led the study. He said: "The ability to study organs outside of the body is delivering new insights into how they work. In this case we've been able to study damaged intestines and instigate repairs which could lead to treatment in a number of conditions." On such condition is short bowel syndrome (SBS) - a condition caused by the dysfunction of sections of the bowel. It can occur in premature babies or in adults due to Crohn's disease or surgery. SBS prevents absorption of vitamins and nutrients and can cause weight loss and is fatal in severe cases. The new research will allow treatments in the form of growth stimulating compounds to be tested ex vivo and perfected before being trialled in the body and eventually in humans. As well as using the basic nutrient base to bridge the gap, the study also experimented with the use of a growth factor called R-spondin 1 to try and speed up growth and make it more successful. Although this caused faster growth it failed to establish the bridge in as uniform a way and fusion was less successful. Professor Woolf added: "In this study we managed to bridge a gap of less than 1mm, but for this to be useful in conditions like short bowel syndrome we'll need to promote growth across much larger distances. Having the ability to test different vitamins and hormones which promote growth opens up many new possibilities for future treatments." The research was funded by the Medical Research Council and The Short Bowel Survivor and Friends Charity. Story Source: The above post is reprinted from materials provided by Manchester University.Note: Materials may be edited for content and length. Journal Reference: Riccardo Coletta, Neil A. Roberts, Francesca Oltrabella, Basem A. Khalil, Antonino Morabito, Adrian S. Woolf. Bridging the gap: functional healing of embryonic small intestineex vivo. Journal of Tissue Engineering and Regenerative Medicine, 2015; DOI: 10.1002/term.2073

Sea Ice in the Greenland Sea

 

As the northern hemisphere experiences the heat of summer, ice moves and melts in the Arctic waters and the far northern lands surrounding it. The Moderate Resolution Imaging Spectroradiometer (MODIS) aboard NASA’s Aqua satellite captured this true-color image of sea ice off Greenland on July 16, 2015.

Large chunks of melting sea ice can be seen in the sea ice off the coast, and to the south spirals of ice have been shaped by the winds and currents that move across the Greenland Sea. Along the Greenland coast, cold, fresh melt water from the glaciers flows out to the sea, as do newly calved icebergs. Frigid air from interior Greenland pushes the ice away from the shoreline, and the mixing of cold water and air allows some sea ice to be sustained even at the height of summer.

According to observations from satellites, 2015 is on track to be another low year for arctic summer sea ice cover. The past ten years have included nine of the lowest ice extents on record. The annual minimum typically occurs in late August or early September. The amount of Arctic sea ice cover has been dropping as global temperatures rise. The Arctic is two to three times more sensitive to temperature changes as the Earth as a whole.

Image Credit: NASA/Jeff Schmaltz, MODIS Land Rapid Response Team, NASA GSFC

Last Updated: Aug. 24, 2015

Editor: Sarah Loff